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Summary[edit | edit source]

  • pan ID?: SAUPAN004913000
  • symbol?: gatD
  • synonym:
  • description?: glutamine amidotransferase

      descriptions from strain specific annotations:

    • glutamine amidotransferase
    • type 1 glutamine amidotransferase
    • CobB/CobQ-like glutamine amidotransferase
    • cobyric acid synthase
    • cobyric acid synthase, putative
    • adenosylcobyric acid synthase (glutamine-hydrolyzing)
    • CobB/CobQ domain-containing protein glutamine amidotransferase
    • CobB/CobQ-like glutamine amidotransferase domain-containing protein
    • cobB/CobQ-like glutamine amidotransferase domain protein
    • cobyric acid synthase CobQ
    • putative amidotransferase, putative cobyricacid synthase
  • strand?: -
  • coordinates?: 5102349..5103080
  • synteny block?: BlockID0038190
  • occurrence?: in 100% of 34 strains

gatD : lipid II isoglutaminyl synthase glutamine amidotransferase subunit [1]

• A crystal structure is available : 6GS2

During cell wall synthesis, the staphylococcal peptidoglycan precursor Lipid II is sequestered at the inner leaflet of the cell membrane for final modifications prior to translocation to the extracellular environment. Two final modifications must occur prior to translocation: addition of a pentaglycine crosslink to the peptide stem lysine and an optional amidation of the peptide stem γ-ᴅ-glutamate to generate isoglutamine. The GatD-MurT complex catalyzes the conversion of peptide stem γ-ᴅ-glutamate to isoglutamine. GatD liberates ammonia from L-glutamine and channels it to the MurT subunit which amidates the glutamate α-carboxylate to generate isoglutamine. Most residues are modified and this modification enhances staphylococcal viability and methicillin resistance.

Orthologs[edit | edit source]

    COL:
    N315:
    NCTC8325:
    Newman:
    USA300_FPR3757:
    04-02981:
    SA2981_1847 (cobQ)
    08BA02176:
    C248_1964
    11819-97:
    MS7_1926
    6850:
    RSAU_001778 (cobQ)
    71193:
    ST398NM01_1984
    ECT-R 2:
    ECTR2_1762
    ED133:
    SAOV_1990
    ED98:
    SAAV_1956
    HO 5096 0412:
    SAEMRSA15_17980
    JH1:
    SaurJH1_1979
    JH9:
    SaurJH9_1945
    JKD6008:
    SAA6008_01911
    JKD6159:
    SAA6159_01822
    JSNZ:
    JSNZ_001921
    LGA251:
    SARLGA251_17730
    M013:
    M013TW_1927
    MRSA252:
    SAR1982
    MSHR1132:
    SAMSHR1132_17350
    MSSA476:
    SAS1813
    Mu3:
    SAHV_1876
    Mu50:
    SAV1891
    MW2:
    MW1832
    RF122:
    SAB1823c
    ST398:
    SAPIG1984
    T0131:
    SAT0131_02016 (clpP)
    TCH60:
    HMPREF0772_11252
    TW20:
    SATW20_18850
    USA300_TCH1516:
    USA300HOU_1889
    VC40:
    SAVC_08715

Genome Viewer[edit | edit source]

COL
N315
NCTC8325
Newman
USA300_FPR3757

Alignments[edit | edit source]

  • alignment of orthologues:
    CLUSTAL format alignment by MAFFT L-INS-i (v7.307)


    COL             MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGG
    N315            MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGG
    NCTC8325        MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGG
    Newman          MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGG
    USA300_FPR3757  MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGG
                    ************************************************************

    COL             GSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDF
    N315            GSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDF
    NCTC8325        GSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDF
    Newman          GSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDF
    USA300_FPR3757  GSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDF
                    ************************************************************

    COL             YTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHY
    N315            YTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHY
    NCTC8325        YTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHY
    Newman          YTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHY
    USA300_FPR3757  YTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHY
                    ************************************************************

    COL             KNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQK
    N315            KNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQK
    NCTC8325        KNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQK
    Newman          KNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQK
    USA300_FPR3757  KNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQK
                    ************************************************************

    COL             KSR
    N315            KSR
    NCTC8325        KSR
    Newman          KSR
    USA300_FPR3757  KSR
                    ***

  1. Daniela Münch, Terry Roemer, Sang Ho Lee, Marianne Engeser, Hans Georg Sahl, Tanja Schneider
    Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus.
    PLoS Pathog: 2012, 8(1);e1002509
    [PubMed:22291598] [WorldCat.org] [DOI] (I p)
    Erik R Nöldeke, Lena M Muckenfuss, Volker Niemann, Anna Müller, Elena Störk, Georg Zocher, Tanja Schneider, Thilo Stehle
    Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.
    Sci Rep: 2018, 8(1);12953
    [PubMed:30154570] [WorldCat.org] [DOI] (I e)
    Maria D Barbuti, Ine S Myrbråten, Danae Morales Angeles, Morten Kjos
    The cell cycle of Staphylococcus aureus: An updated review.
    Microbiologyopen: 2023, 12(1);e1338
    [PubMed:36825883] [WorldCat.org] [DOI] (I p)